Oligomers of the Prion Protein Fragment 106−126 Are Likely Assembled from β-Hairpins in Solution, and Methionine Oxidation Inhibits Assembly without Altering the Peptide’s Monomeric Conformation

2010 ◽  
Vol 132 (2) ◽  
pp. 532-539 ◽  
Author(s):  
Megan Grabenauer ◽  
Chun Wu ◽  
Patricia Soto ◽  
Joan-Emma Shea ◽  
Michael T. Bowers
Keyword(s):  
Prion Protein ◽  
Methionine Oxidation ◽  
Protein Fragment

A Unique Functional Feature of the Recombinant Bovine Prion Protein Fragment

2014 ◽  
Author(s):  
Ying Zhai ◽  
Na Li ◽  
Dachuan Zhang ◽  
Qi Li ◽  
Guoping Zhou ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Fragment ◽  
Functional Feature

scholarly journals Self-Replication of Prion Protein Fragment 89-230 Amyloid Fibrils Accelerated by Prion Protein Fragment 107-143 Aggregates

2020 ◽  
Vol 21 (19) ◽  
pp. 7410
Author(s):  
Tomas Sneideris ◽  
Mantas Ziaunys ◽  
Brett K.-Y. Chu ◽  
Rita P.-Y. Chen ◽  
Vytautas Smirnovas
Keyword(s):  
Prion Protein ◽  
Disease Transmission ◽  
Amyloid Fibrils ◽  
The Self ◽  
Transmissible Spongiform Encephalopathies ◽  
Protein Fragment ◽  
Spongiform Encephalopathies ◽  
Amyloid Fibril Formation ◽  
Amyloid Aggregates ◽  
Self Replication

Prion protein amyloid aggregates are associated with infectious neurodegenerative diseases, known as transmissible spongiform encephalopathies. Self-replication of amyloid structures by refolding of native protein molecules is the probable mechanism of disease transmission. Amyloid fibril formation and self-replication can be affected by many different factors, including other amyloid proteins and peptides. Mouse prion protein fragments 107-143 (PrP(107-143)) and 89-230 (PrP(89-230)) can form amyloid fibrils. β-sheet core in PrP(89-230) amyloid fibrils is limited to residues ∼160–220 with unstructured N-terminus. We employed chemical kinetics tools, atomic force microscopy and Fourier-transform infrared spectroscopy, to investigate the effects of mouse prion protein fragment 107-143 fibrils on the aggregation of PrP(89-230). The data suggest that amyloid aggregates of a short prion-derived peptide are not able to seed PrP(89-230) aggregation; however, they accelerate the self-replication of PrP(89-230) amyloid fibrils. We conclude that PrP(107-143) fibrils could facilitate the self-replication of PrP(89-230) amyloid fibrils in several possible ways, and that this process deserves more attention as it may play an important role in amyloid propagation.

scholarly journals Detection of the GPI-anchorless prion protein fragment PrP226* in human brain

BMC Neurology ◽  
2013 ◽  
Vol 13 (1) ◽  
Author(s):  
Eva Dvorakova ◽  
Tanja Vranac ◽  
Olga Janouskova ◽  
Maja Černilec ◽  
Simon Koren ◽  
...  
Keyword(s):  
Human Brain ◽  
Prion Protein ◽  
Protein Fragment

Creutzfeldt-Jakob disease in a patient with an R208H mutation of the prion protein gene (PRNP) and a 17-kDa prion protein fragment

2005 ◽  
Vol 109 (4) ◽  
pp. 443-448 ◽  
Author(s):  
Sigrun Roeber ◽  
Bjarne Krebs ◽  
Manuela Neumann ◽  
Otto Windl ◽  
Inga Zerr ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Gene ◽  
Prion Protein Gene ◽  
Protein Fragment ◽  
Jakob Disease

Haem oxygenase-1 mRNA induction by a prion protein fragment in rat astroglial cells

1995 ◽  
Vol 31 ◽  
pp. 218
Author(s):  
L. Cantoni ◽  
M. Rizzardini ◽  
R. Carcano ◽  
M. Salmona ◽  
R. Chiesa ◽  
...  
Keyword(s):  
Prion Protein ◽  
Protein Fragment ◽  
Astroglial Cells ◽  
Mrna Induction ◽  
Haem Oxygenase

scholarly journals Fibrillation of N-Terminal Prion Protein Fragment in Presence of Zinc Ions

2018 ◽  
Vol 114 (3) ◽  
pp. 429a
Author(s):  
Maciej B. Gielnik ◽  
Michał Nowakowski ◽  
Aneta Szymańska ◽  
Igor Yu Zhukov ◽  
Wojciech Maria Kwiatek ◽  
...  
Keyword(s):  
Prion Protein ◽  
Zinc Ions ◽  
Protein Fragment

scholarly journals Sulphated glycosaminoglycans prevent the neurotoxicity of a human prion protein fragment

1998 ◽  
Vol 335 (2) ◽  
pp. 369-374 ◽  
Author(s):  
Mar PÉREZ ◽  
Francisco WANDOSELL ◽  
Camilo COLAÇO ◽  
Jesús AVILA
Keyword(s):  
Prion Protein ◽  
Amyloid Fibrils ◽  
Transmissible Spongiform Encephalopathies ◽  
Therapeutic Effects ◽  
Protein Fragment ◽  
Spongiform Encephalopathies ◽  
Sulphated Polysaccharides ◽  
Human Prion Protein ◽  
Sulphated Glycosaminoglycans

Although a number of features distinguish the disease isoform of the prion protein (PrPSc) from its normal cellular counterpart (PrPC) in the transmissible spongiform encephalopathies (TSEs), the neuropathogenesis of these diseases remains an enigma. The amyloid fibrils formed by fragments of human PrP have, however, been shown to be directly neurotoxic in vitro. We show here that sulphated polysaccharides (heparin, keratan and chondroitin) inhibit the neurotoxicity of these amyloid fibrils and this appears to be mediated via inhibition of the polymerization of the PrP peptide into fibrils. This provides a rationale for the therapeutic effects of sulphated polysaccharides and suggests a rapid in vitro functional screen for TSE therapeutics.

Flupirtine partially prevents neuronal injury induced by prion protein fragment and lead acetate

1996 ◽  
Vol 30 (1) ◽  
pp. A38
Author(s):  
Müller Weg ◽  
Perovic S ◽  
Pergande G ◽  
Omoto K ◽  
Ushijima H
Keyword(s):  
Prion Protein ◽  
Lead Acetate ◽  
Neuronal Injury ◽  
Protein Fragment

scholarly journals Distinct Proteinase K-Resistant Prion Protein Fragment in Goats with No Signs of Disease in a Classical Scrapie Outbreak

2011 ◽  
Vol 49 (6) ◽  
pp. 2109-2115 ◽  
Author(s):  
Ilias G. Bouzalas ◽  
Florian Lörtscher ◽  
Chrysostomos I. Dovas ◽  
Anna Oevermann ◽  
Jan P. M. Langeveld ◽  
...  
Keyword(s):  
Prion Protein ◽  
Classical Scrapie ◽  
Proteinase K ◽  
Protein Fragment
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